Comparative Biochemistry of Hemoglobins

Chicken hemoglobin contains two kinds of main components, A I and A II, and their genetic control mechanism in the red blood cells interests us much. Each of these two components consists of two α-and two β-polypeptide chains. As a basic experiment for the study of the primary structure of these α-and β-chains in chicken hemoglobin, the author identified the tryptic peptides obtained from these components and from the chains composing these components by the so-called fingerprinting method. First, component A I and A II were purified by column chromatography with the salt concentration gradient of phosphate buffer using carboxymethyl cellulose as the adsorbent, and subsequently, the α-and β-polypeptide chains were isolated from these components by column chromatography by the elution with ureaformic acid solution using CG-50 (type II) as the adsorbent. The obtained components A I and A II, and the α-and β-polypeptide chains from these components were hydrolyzed with trypsin, and every variety of tryptic digests thus obtained was identified by the fingerprinting method